AOX1_AERPE
ID AOX1_AERPE Reviewed; 815 AA.
AC Q9YDX6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Heme-copper oxidase subunit I+III;
DE EC=1.9.3.-;
GN Name=aoxB; OrderedLocusNames=APE_0793.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RA Wakagi T., Ishikawa R.;
RT "Heme-copper-oxidase.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds a copper B center. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB020482; BAA86072.1; -; Genomic_DNA.
DR EMBL; BA000002; BAA79771.2; -; Genomic_DNA.
DR PIR; C72671; C72671.
DR AlphaFoldDB; Q9YDX6; -.
DR SMR; Q9YDX6; -.
DR STRING; 272557.APE_0793.1; -.
DR EnsemblBacteria; BAA79771; BAA79771; APE_0793.1.
DR KEGG; ape:APE_0793.1; -.
DR PATRIC; fig|272557.25.peg.572; -.
DR eggNOG; arCOG01237; Archaea.
DR OMA; FWGKMSF; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.120.80; -; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR Pfam; PF00510; COX3; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
DR PROSITE; PS50253; COX3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..815
FT /note="Heme-copper oxidase subunit I+III"
FT /id="PRO_0000183466"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 708..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..811
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..467
FT /note="COX1"
FT REGION 545..815
FT /note="COX3"
FT BINDING 70
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 252
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 297
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 298
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 383
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 385
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 248..252
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 815 AA; 90860 MW; 9E911C57BEF9BBE2 CRC64;
MVSRLRGFLA WVYRWITTTD HKDIGLLYLV TSIAFLLIAG SLALLFRVQL AIPKSNFLTG
DAYYEAVTVH GLIMLLWFAS PFAFGLANYI VPLQIGARDL AFPRLNALSY WLYLLSGLVL
LASFFTESGA PNVGWTLYAP LTARIYTPGI GLDLAALAIF LFSLSVTLGT INFLVTIAAM
RAPGIGWFKM PMFTWSILFT VILMLWAFPP LMVGGALLLL DRNLGTEFFL NPAGGALLWD
HLFWFFGHPE VYILLFPALG AMADVISTFS GKPIYAKRYI LTAFLIATII SFVVWMHHMF
ITGTNIYTRL FYSITTILIS IPFEMAVMSF IFTLYKGRLV YTVPMLFAVG ALLNFIIGGS
TGVYLGSIAI DRGFRGTYWV VAHFHYILVG TVTLGLIAGL YYWWPKITGR TYSERLGKIH
FALAMLGVAL TFLPQFALMD MPRRYFTYDI PEWVPLNQLS TLGAFIFGGS MAIGLVNFLY
SLVKGGSAAP NPWNSWTLEW FTNSPPPKHN FDGVPVVRKD NTVVFVSEEA LSKYGKDAIV
EGRVDVSNVP LSGGQSHSSH GLTHHGTTDP LVLAAGLTLA LFGLFVSKPL SYLGAIVFLL
SLARWLWKDV KNVFAEELPG YVEHWPFPKD KIRSAMWVFI ASEVATFGSI FSAYFFIRFN
PVGKFLTEAW PPGYLVHDVN VGLINTIILF TGTMLFTLAY LGVKRDNYLI TLSGLLGTLF
MAIYFLTVKY FEWKELLIAG LGLDAGMYMQ AYYVTTGAHA LHVILGVLAT TYLLVKLFNG
NLRGRQALSE VLAVGIYWGI VEIVWTLVFP LYYLV
